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5LUK

Structure of a double variant of cutinase 2 from Thermobifida cellulosilytica

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 301
ChainResidue
AARG187
AASN191
AGLN239
AARG257

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 302
ChainResidue
ATHR178
AHIS209

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 303
ChainResidue
AHOH495
ATYR61
ASER131
AMET132

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 304
ChainResidue
AVAL25
AASP111
AALA112
AHOH404
AHOH507
AHOH534

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 305
ChainResidue
AARG32
AALA35
APHE38
AHOH518
AHOH530
AHOH580

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LAVMGHSMGG
ChainResidueDetails
ALEU125-GLY134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q47RJ6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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